Interactions between beta-lactoglobulin and aroma compounds: different binding behaviors as a function of ligand structure.
Interactions between beta-lactoglobulin (BLG) in its monomeric form and a wide range of aroma compounds were investigated by Fourier transform infrared (FT-IR) and 2D nuclear magnetic resonance (NMR) spectroscopies. A screening of the ligands was carried out by FT-IR through the amide I region changes of BLG upon binding. The location of two binding sites was determined by 2D NMR from the study of 10 selected ligands with different structures. All of the data suggest at least two binding behaviors as a function of the chemical class, the hydrophobicity, or the structure of the ligands. The binding of the elongated aroma compounds, such as 2-nonanone or ethyl pentanoate, within the central cavity involves residues located at the entrance of the calyx and Trp19. The binding onto the protein surface of aroma compounds that have or adopt a compact structure occurs in a site located between strand beta-G, alpha helix, and strand beta-I.
Tavel
Laurette
L
INRA, UMR 1129 FLAVIC, F-21000 Dijon, France.
Andriot
Isabelle
I
Moreau
Céline
C
Guichard
Elisabeth
E
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D057927:Hydrophobic and Hydrophilic Interactions; D007782:Lactoglobulins / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D009930:Organic Chemicals / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017550:Spectroscopy, Fourier Transform Infrared; D013329:Structure-Activity Relationship
D007782:Lactoglobulins; D008024:Ligands; D009930:Organic Chemicals